Differences in prostaglandin E2, prostaglandin F2α and prostacyclin contents and their response to thyrotrophin stimulation and in prostaglandin-stimulated cyclic AMP response in normal and Graves's thyroid slices

1983 ◽  
Vol 98 (3) ◽  
pp. 357-363 ◽  
Author(s):  
Nobuyuki Takasu ◽  
Kazunori Takahashi ◽  
Tatsuro Ishigami ◽  
Takashi Yamada ◽  
Seiya Sato
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E2 ◽  
Prostaglandin F2α ◽  
Human Thyroid ◽  
Prostaglandin E ◽  
Normal Thyroid ◽  
Cyclic Amp Synthesis

The human thyroid contained prostaglandin (PG) E2, PGF2α and 6-oxo-PGF1α, an end-metabolite of prostacyclin (PGI2), the 6-oxo-PGF1α content being the highest of these prostaglandins. Graves's thyroid contained a significantly higher amount of PGF2α and lower amounts of PGE2 and 6-oxo-PGF1α than the normal thyroid. Thyrotrophin acutely augmented the thyroid contents of PGE2, PGF2α and 6-oxo-PGF1α. The TSH-stimulated increases in PGE2 and 6-oxo-PGF1α were lower but the TSH-stimulated increase in PGF2α was significantly higher in Graves's thyroid than in the normal thyroid. Prostaglandin E2 and PGI2 stimulated human thyroid cyclic AMP synthesis, with the magnitudes of PGE2-and PGI2-stimulated increases in cyclic AMP being equal in normal and Graves's thyroid. Prostaglandin E2α did not stimulate cyclic AMP synthesis significantly. These results provide evidence that prostaglandins play important roles in thyroid physiology and the pathophysiology of Graves's disease.

Thyrotrophin and prostaglandin E2 increase calmodulin levels and cyclic AMP phosphodiesterase activity in cultured porcine thyroid cells

1988 ◽  
Vol 117 (1) ◽  
pp. 109-114 ◽  
Author(s):  
N. Takasu ◽  
T. Yamada ◽  
Y. Shimizu
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E2 ◽  
Prostaglandin E ◽  
Maximal Velocity ◽  
Phosphodiesterase Activity ◽  
Dibutyryl Camp ◽  
Camp Phosphodiesterase ◽  
Thyroid Cells ◽  
Michaelis Constants ◽  
Camp Hydrolysis

ABSTRACT Thyrotrophin (TSH) and prostaglandin E2 (PGE2) increased cellular cyclic AMP (cAMP), calmodulin levels and cAMP phosphodiesterase activity in cultured porcine thyroid cells. Dibutyryl cAMP (dbcAMP), a stable analogue of cAMP, increased calmodulin levels and cAMP phosphodiesterase activity. These results indicate that TSH- and PGE2-stimulated increases in calmodulin are mediated by cAMP. This increased concentration of calmodulin in turn stimulates cAMP phosphodiesterase. Double reciprocal plots of cAMP hydrolysis yielded two apparent Michaelis constants (Km); the lower in the 1 μmol/l and the higher in the 10 μmol/l range. Thyrotrophin, PGE2 and dbcAMP increased the values of maximal velocity without changing the Km values. J. Endocr. (1988) 117, 109–114

Effect of phosphodiesterase inhibitors on bradykinin-mediated prostaglandin E2 and cyclic amp synthesis in renal papillary collecting tubule cells

1985 ◽  
Vol 34 (9) ◽  
pp. 1565-1569 ◽  
Author(s):  
Leslie A. Spry ◽  
Neville S. Rapp ◽  
David L. Thomasson ◽  
Terry V. Zenser ◽  
Bernard B. Davis
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E2 ◽  
Phosphodiesterase Inhibitors ◽  
Collecting Tubule ◽  
Tubule Cells ◽  
Cyclic Amp Synthesis

EFFECTS OF PROSTAGLANDIN E2 AND DIBUTYRYL CYCLIC AMP ON THE HISTAMINE-INDUCED PRODUCTION OF CORTISOL AND CORTICOSTERONE IN ISOLATED CANINE ADRENAL CELLS

1979 ◽  
Vol 82 (2) ◽  
pp. 275-277 ◽  
Author(s):  
T. HIROSE ◽  
I. MATSUMOTO ◽  
T. AIKAWA
Keyword(s):  
Cyclic Amp ◽  
Prostaglandin E2 ◽  
Prostaglandin E ◽  
Dibutyryl Cyclic Amp ◽  
Adrenocortical Cells ◽  
Adrenal Cells ◽  
Individual Effects

SUMMARY The steroidogenic effect of histamine in isolated adrenocortical cells of the dog was investigated in the presence of prostaglandin E2 (PGE2) and/or dibutyryl cyclic AMP (dbcAMP) in the medium. The effect of histamine, in combination with PGE2, was less than their total individual effects in the production of cortisol, but not of corticosterone. With dbcAMP the effect was just equal to them. However, the combination of histamine, PGE2 and dbcAMP showed an increase twice that of their total individual effects in the production of both steroids. These results indicate that, in the dog, histamine, PGE2 and dbcAMP may act synergistically in the adrenocortical cells.

CHANGES IN MEMBRANE POTENTIAL OF CULTURED PORCINE AND HUMAN THYROID CELLS IN RESPONSE TO THYROTROPHIN AND OTHER AGENTS

1981 ◽  
Vol 88 (2) ◽  
pp. 187-NP ◽  
Author(s):  
J. R. BOURKE ◽  
K. L. CARSELDINE ◽  
S. H. FERRIS ◽  
G. J. HUXHAM ◽  
S. W. MANLEY
Keyword(s):  
Membrane Potential ◽  
Cyclic Amp ◽  
Human Thyroid ◽  
Resting Membrane Potential ◽  
Prostaglandin E ◽  
Follicular Cells ◽  
Thyroid Cells ◽  
Enhanced Sensitivity ◽  
Long Acting ◽  
Cells Cultured

Thyrotrophin (TSH), cyclic AMP, cyclic GMP and 1-methyl-3-isobutyl-xanthine (MIX) promoted the reassociation of isolated porcine and human thyroid cells into follicular structures in culture and stimulated the uptake of radio-iodide. Monolayer cells were present in all cultures, but in decreasing proportions as the concentration of stimulator was increased. The resting membrane potential of porcine thyroid cells cultured for 4 days in the presence of TSH was −54 ± 3·6 (mean ± s.d.) mV for follicular cells and −31 ± 2·6 mV for monolayer cells. In the absence of TSH, only monolayer cells were present and their membrane potential was −24 ± 2·0 mV. Removal of hormone by washing resulted in hyperpolarization to −70 ± 2·9 mV (follicular cells) or −59 ± 3·4 mV (monolayer cells). Subsequent replacement of TSH, or addition of cyclic AMP, MIX, prostaglandin E1 (PGE1) or long-acting thyroid stimulator immunoglobulin resulted in depolarization of previously hyperpolarized cells, to approximately the membrane potential observed before washing. Incubation in MIX resulted in enhanced sensitivity to the depolarizing effect of TSH. Cells cultured in the absence of TSH were unresponsive to TSH or other stimulators. The membrane potential of human thyroid cells behaved similarly in response to TSH, to hormone removal and replacement, and to MIX and PGE1.

Dependence of Platelet Adenyl Cyclase System on Oxidative Phosphorylation

1975 ◽  
Vol 34 (01) ◽  
pp. 042-049 ◽  
Author(s):  
Shuichi Hashimoto ◽  
Sachiko Shibata ◽  
Bokro Kobayashi
Keyword(s):  
Cyclic Amp ◽  
Oxidative Phosphorylation ◽  
Sodium Succinate ◽  
Potassium Cyanide ◽  
Adenyl Cyclase ◽  
Mitochondrial Oxidative Phosphorylation ◽  
Adenyl Cyclase Activity ◽  
Intact Rabbit ◽  
Adenyl Cyclase System ◽  
Cyclic Amp Synthesis

SummaryThe radioactive adenosine 3′,5′-monophosphate (cyclic AMP) level derived from 8-14C adenine in intact rabbit platelets decreased in the presence of mitochondrial inhibitor (potassium cyanide) or uncoupler (sodium azide), and markedly increased by the addition of NaF, monoiodoacetic acid (MIA), or 2-deoxy-D-glucose. The stimulative effect of the glycolytic inhibitors was distinctly enhanced by the simultaneous addition of sodium succinate. MIA did neither directly stimulate the adenyl cyclase activity nor inhibit the phosphodiesterase activity. These results suggest that cyclic AMP synthesis in platelets is closely linked to mitochondrial oxidative phosphorylation.

Interaction between parathyroid hormone and prostaglandin E1 on cyclic AMP metabolism in rat kidney

1980 ◽  
Vol 93 (3) ◽  
pp. 339-345 ◽  
Author(s):  
Naokazu Nagata ◽  
Yuriko Ono ◽  
Narimichi Kimura
Keyword(s):  
Parathyroid Hormone ◽  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Rat Kidney ◽  
Prostaglandin E ◽  
Cortical Tissue ◽  
Newborn Rat ◽  
Simultaneous Addition ◽  
Renal Cortical Tissue ◽  
Subsequent Addition

Abstract. The interaction between parathyroid hormone (PTH) and prostaglandin E1 (PGE1) in influencing cyclic AMP metabolism in rat renal cortical tissue was examined. PTH and PGE1 stimulated additively the adenylate cyclase activity in the homogenate of the tissue. Both PTH and PGE1 enhanced the level of cyclic AMP in the incubated renal cortical tissue, but the effect of their simultaneous addition did not exceed the effect induced by PTH alone. Cyclic AMP accumulated in the incubation medium by stimulation by PTH was decreased by the simultaneous addition of PGE1. When the tissue was pre-incubated for 30 min with 2 to 10 μg/ml of PGE1, the magnitude of the increase of cyclic AMP caused by PTH subsequently added was lessened. However, the response to PTH of adenylate cyclase preparation obtained from the homogenate of PGE1-pre-treated tissue was not decreased. When first PTH was added to the incubating renal cortical tissue, the subsequent addition of PGE1 accelerated the decrease of cyclic AMP content in the tissue and decreased the amount of cyclic AMP released from the tissue. The interaction of PTH and PGE1 on cyclic AMP metabolism in the renal cortical tissue was in contrast to that seen in newborn rat calvaria where PGE1 and PTH acted additively in enhancing the level of cyclic AMP.

scholarly journals Expression of a Gαs/Gαi Chimera That Constitutively Activates Cyclic AMP Synthesis

1989 ◽  
Vol 264 (10) ◽  
pp. 5687-5693
Author(s):  
C W Woon ◽  
S Soparkar ◽  
L Heasley ◽  
G L Johnson
Keyword(s):  
Cyclic Amp ◽  
Cyclic Amp Synthesis

scholarly journals Interactions between adenylate cyclase and the yeast GTPase-activating protein IRA1.

1991 ◽  
Vol 11 (9) ◽  
pp. 4591-4598 ◽  
Author(s):  
M R Mitts ◽  
J Bradshaw-Rouse ◽  
W Heideman
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Adenylate Cyclase System ◽  
Gtpase Activating Protein ◽  
Yeast Saccharomyces Cerevisiae ◽  
Strong Candidate ◽  
Sepharose 4B ◽  
Stimulation Of ◽  
Cyclic Amp Synthesis

The adenylate cyclase system of the yeast Saccharomyces cerevisiae contains many proteins, including the CYR1 polypeptide, which is responsible for catalyzing the formation of cyclic AMP from ATP, RAS1 and RAS2 polypeptides, which mediate stimulation of cyclic AMP synthesis by guanine nucleotides, and the yeast GTPase-activating protein analog IRA1. We have previously reported that adenylate cyclase is only peripherally bound to the yeast membrane. We have concluded that IRA1 is a strong candidate for a protein involved in anchoring adenylate cyclase to the membrane. We base this conclusion on the following criteria: (i) a disruption of the IRA1 gene produced a mutant with very low membrane-associated levels of adenylate cyclase activity, (ii) membranes made from these mutants were incapable of binding adenylate cyclase in vitro, (iii) IRA1 antibodies inhibit binding of adenylate cyclase to the membrane, and (iv) IRA1 and adenylate cyclase comigrate on Sepharose 4B.

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